Purification of pseudouridylate synthetase I from Salmonella typhimurium
- 1 December 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 5 (12) , 4523-4536
- https://doi.org/10.1093/nar/5.12.4523
Abstract
Pseudouridylate synthetase from Salmonella typhimurium has been purified 1,000 fold and is about 90% pure. The enzyme has a molecular weight of 50,000 daltons. In the presence of tRNA there is a change in molecular weight from 50.000 to 100.000. This change does not seem to be due to the formation of a tRNA-enzyme complex but rather to a tRNA induced dimerization. Other properties of the enzyme are described.Keywords
This publication has 18 references indexed in Scilit:
- Cysteine transfer RNA of Escherichia coli: Nucleotide sequence and unusual metabolic properties of the 3′ C-C-A terminusJournal of Molecular Biology, 1977
- Biosynthesis of pseudouridine in the in vitro transcribed tRNATyr precursorFEBS Letters, 1977
- Dual-control of the tryptophan operon is mediated by both tryptophanyl-tRNA synthetase and the repressorJournal of Molecular Biology, 1976
- Primary structure of tRNALysof E. coli BNucleic Acids Research, 1975
- The Nucleotide Sequence of a Threonine Transfer Ribonucleic Acid from Escherichia coliJournal of Biological Chemistry, 1974
- Primary structure of E. coli alanine transfer RNA: Relation to the yeast phenylalanyl tRNA synthetase recognition siteBiochemical and Biophysical Research Communications, 1974
- Pleiotropy of hisT Mutants Blocked in Pseudouridine Synthesis in tRNA: Leucine and Isoleucine-V aline OperonsProceedings of the National Academy of Sciences, 1974
- Mutants of Escherichia coli Thermosensitive for the Synthesis of Transfer RNAProceedings of the National Academy of Sciences, 1973
- Histidine regulation in salmonella typhimurium. XIV. Interaction of the histidyl transfer ribonucleic acid synthetase with histidine transfer ribonucleic acid.1972
- Mutant tRNAHis Ineffective in Repression and Lacking Two Pseudouridine ModificationsNature New Biology, 1972